Journal of Physical Chemistry B, Vol.106, No.20, 5275-5280, 2002
Solution structure of a type 1 H antigen trisaccharide at a micellar surface: NMR relaxation and molecular dynamics simulation studies
The conformation and dynamics of the type 1 H trisaccharide alpha-L-Fucp-(1-->2)-beta-D-Galp-(1-->3)-beta-D-GlcpNAc has been studied as a glycolipid (GL) in a micellar sodium dodecyl sulfate-d(25) (SDS)/D2O solution. Carbon-13 spin-lattice (T-1) and spin-spin (T-2) relaxation time measurements of the GL in the SIDS micelles were carried out at two magnetic field strengths, namely, 11.7 and 14.1 T employing 2D NMR techniques. H-1,H-1 NOESY spectra at the higher field were used to obtain proton-proton cross-relaxation rates. A molecular dynamics simulation of the trisaccharide with explicit water was performed for 3 ns to generate a 3D molecular model. From the C-13 NMR relaxation data, a reorientational correlation time was derived for the GL with tau(M) = 1.7 ns as well as a generalized order parameter, S-2 = 0.86, using the "model-free" formalism of Lipari and Szabo. Proton-proton distances were calculated from the experimental NMR data. A comparison based on these distances between the GL at the micellar surface and the trisaccharide simulated in water revealed a similar trans-glycosidic distance at the (1-->2)-linkage whereas for the corresponding proton pair at the (1-->3)-linkage a larger difference was present. On the basis of the Stokes-Einstein relationship for the SIDS micelle and the assumption that the GL has a lateral diffusion coefficient similar to that of the SDS molecules on the micellar surface, a reorientational correlation time was estimated close to that found by experiment. The latter finding stresses that lateral diffusion contributes an important part in the reorientational motion of the GL.